Structural evidence for guanidine-protein side chain interactions: crystal structure of CutA from Pyrococcus horikoshii in 3 M guanidine hydrochloride

Biochemical and Biophysical Research Communications
Yoshikazu TanakaIzumi Kumagai

Abstract

This study was carried out to investigate the structural perturbation of the protein's local structure by the denaturants under non-denaturing conditions. Crystal structure of CutA from an archaeon Pyrococcus horikosii (PhoCutA), a heavy-metal binding protein, was determined at 1.6-angstroms resolution in the presence of 3 M guanidine HCl (GdnHCl). Native PhoCutA has a large number of short intramolecular hydrogen bonds and salt bridges on the protein surface, of which greater than 90% of hydrogen bonds and all salt bridges were retained in 3 M GdnHCl. Hydrogen bonds that disappeared in the GdnHCl crystal structure were mainly located on the protein surface, especially around the structurally perturbed loop, suggesting interactions between peptide groups and GdnHCl. Only a few GdnH+ ions were observed in the crystal structure, although none at the surface, of the protein. Two GdnH+ ions were observed in the center of the trimeric structure, replacing water molecules, and were hydrogen bonded with Asp84 and Asp86 of each chain. The exterior loop from Tyr39 to Lys44, including Trp40-Trp41, was perturbed structurally. Decreases in temperature factors were observed in beta strand 5 and the N terminus of helix 3. These results sugge...Continue Reading

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Citations

Feb 16, 2006·Journal of Fluorescence·Sónia GonçalvesCarlota Saldanha
Nov 6, 2010·Protein Engineering, Design & Selection : PEDS·Beatriz MaestroJesús M Sanz
May 17, 2005·Protein Expression and Purification·Matsujiro IshibashiTsutomu Arakawa
Mar 1, 2007·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Nadeem JavidRoland Winter
Oct 10, 2007·Molecular Biology Reports·Jingchun YangLong Yu
Apr 6, 2007·Protein Expression and Purification·Tsutomu ArakawaDaisuke Ejima

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